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Conserved domains on  [gi|145336886|ref|NP_176215|]
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Adaptor protein complex AP-1, gamma subunit [Arabidopsis thaliana]

Protein Classification

AP-1 complex subunit gamma( domain architecture ID 12024706)

AP-1 complex subunit gamma is a subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Adaptin_N pfam01602
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
26-580 3.42e-164

Adaptin N terminal region; This family consists of the N terminal region of various alpha, beta and gamma subunits of the AP-1, AP-2 and AP-3 adaptor protein complexes. The adaptor protein (AP) complexes are involved in the formation of clathrin-coated pits and vesicles. The N-terminal region of the various adaptor proteins (APs) is constant by comparison to the C-terminal which is variable within members of the AP-2 family; and it has been proposed that this constant region interacts with another uniform component of the coated vesicles.


:

Pssm-ID: 396262 [Multi-domain]  Cd Length: 523  Bit Score: 487.90  E-value: 3.42e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886   26 ERAVVRKECAAIRASINENDQdYRHRDLAKLMFIHMLGYPTHFGQMECLKLIASPGFPEKRIGYLGLMLLLDERQEVLML 105
Cdd:pfam01602   1 EEKRIQQELARILNSFRDDPR-KKKNAVKKLLYLIMLGEDISFLFFEVVKLVASKDFTLKRLGYLYLMLLAEESPDLAIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  106 VTNSLKQDLNHTNQYIVGLALCALGNICSAEMARDLAPEVERLLQFRDPNIRKKAALCAIRIIRKVPDLSENFINPGAAL 185
Cdd:pfam01602  80 VTNSIQKDLQSPNQLIRGLALRTLSCIRVPELARDLAPDIKKLLVDRSPYVRKKAALAILKLYRKSPDLVRDFVPELKEL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  186 LKEKHHGVLITGVHLCTEICKVSSEALeyfrkKCTEGLVKTLRDIANspyspeydvagITDPFLHIRLLKLLRVLGQGD- 264
Cdd:pfam01602 160 LSDKDPGVQSAAVALLYEICKNDRLYL-----KLLPLLFRRLCNLLG-----------VLNPWLQVKILRLLTRLAPLDp 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  265 ADASDCMNDILAQVAsktesnkNAGNAILYECVQTIMSIEENGGLRVLAINILGKFLSNRDNNIRYVALNMLMRSLTVDS 344
Cdd:pfam01602 224 LLPKELLEDLLNLLQ-------NSNNAVLYETANTIVHLAPAPELIVLAVNALGRLLSSPDENLRYVALRNLNKIVMKEP 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  345 QAVQrHRATILECVK-DSDASIQKRALELIYLLVNENNVKPLAKELIEYL-EVSEQDFKGDLTAKICSIVEKFAPEKIWY 422
Cdd:pfam01602 297 KAVQ-HLDLIIFCLKtDDDISIRLRALDLLYALVNESNVKEIVKELLKYVhEIADPDFKIELVRAIGRLAEKFPTDAEWY 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  423 IDQMLKVLSEAGTYVKEDVWHALIVVITNAPDLHGYTVRALYRALHTSfEQETLVRVAIWCIGEYADLLVNNagmldled 502
Cdd:pfam01602 376 LDVLLDLLSLAGSYVVDEIVEVIRDIIQNVPELREYILEHLCELLEDI-ESPEALAAALWILGEYGELIPNG-------- 446
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  503 pitvteSDAVDVVENAI-KHHLSDVTTKAMALIALLKISSRFPSCS--ERVKSIIGQ--NKGSFVLELQQRSLEFSSVIQ 577
Cdd:pfam01602 447 ------SSPPDLLRSILeVFVLESAKVRAAALTALAKLGLTSPEETtqNLIIQLLLTlaTQDSLDLEVRDRAVEYLRLLS 520

                  ...
gi 145336886  578 KHQ 580
Cdd:pfam01602 521 LAD 523
Alpha_adaptinC2 smart00809
Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link ...
751-859 5.32e-33

Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Gamma-adaptin is a subunit of the golgi adaptor. Alpha adaptin is a heterotetramer that regulates clathrin-bud formation. The carboxyl-terminal appendage of the alpha subunit regulates translocation of endocytic accessory proteins to the bud site. This Ig-fold domain is found in alpha, beta and gamma adaptins and consists of a beta-sandwich containing 7 strands in 2 beta-sheets in a greek-key topology.. The adaptor appendage contains an additional N-terminal strand.


:

Pssm-ID: 197886 [Multi-domain]  Cd Length: 104  Bit Score: 122.74  E-value: 5.32e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886   751 AFESSSLKIEFNFTKQSENpqtTDIVANFINLTPNVYTEFLFQAAVPKFLQLHLDPASSNSLPANGNIKQTMRVTNsqKG 830
Cdd:smart00809   1 AYEKNGLQIGFKFERRPGL---IRITLTFTNKSPSPITNFSFQAAVPKSLKLQLQPPSSPTLPPGGQITQVLKVEN--PG 75
                           90       100
                   ....*....|....*....|....*....
gi 145336886   831 KKPIVMRMRVGYKINGKDVLEEGQINNFP 859
Cdd:smart00809  76 KFPLRLRLRLSYLLGGSAVTEQGDVLKFP 104
KAR9 super family cl25816
Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal ...
596-756 8.68e-03

Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal protein required for karyogamy, correct positioning of the mitotic spindle and for orientation of cytoplasmic microtubules. KAR9 localizes at the shmoo tip in mating cells and at the tip of the growing bud in anaphase.


The actual alignment was detected with superfamily member pfam08580:

Pssm-ID: 430088 [Multi-domain]  Cd Length: 684  Bit Score: 39.81  E-value: 8.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  596 ATFSGRRAGS--LPASVSTSGKSPLGIPNGVAKAAAPLvdllDLGSDDTPAPTSSSNnflqdlLGVDLSQPSAQPGAMQP 673
Cdd:pfam08580 448 KTPSSRRGSSfdFGSSSERVINSKLRRESKLPQIASTL----KQTKRPSKIPRASPN------HSGFLSTPSNTATSETP 517
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  674 SQAGADILMDLLSIGTPAPVQNGSANGDLLSIQDNNAPIAPSLTSPTaPSSMMDLLDGFGPTPPKSEDKSAAYPSIVAFE 753
Cdd:pfam08580 518 TPALRPPSRPQPPPPGNRPRWNASTNTNDLDVGHNFKPLTLTTPSPT-PSRSSRSSSTLPPVSPLSRDKSRSPAPTCRSV 596

                  ...
gi 145336886  754 SSS 756
Cdd:pfam08580 597 SRA 599
 
Name Accession Description Interval E-value
Adaptin_N pfam01602
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
26-580 3.42e-164

Adaptin N terminal region; This family consists of the N terminal region of various alpha, beta and gamma subunits of the AP-1, AP-2 and AP-3 adaptor protein complexes. The adaptor protein (AP) complexes are involved in the formation of clathrin-coated pits and vesicles. The N-terminal region of the various adaptor proteins (APs) is constant by comparison to the C-terminal which is variable within members of the AP-2 family; and it has been proposed that this constant region interacts with another uniform component of the coated vesicles.


Pssm-ID: 396262 [Multi-domain]  Cd Length: 523  Bit Score: 487.90  E-value: 3.42e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886   26 ERAVVRKECAAIRASINENDQdYRHRDLAKLMFIHMLGYPTHFGQMECLKLIASPGFPEKRIGYLGLMLLLDERQEVLML 105
Cdd:pfam01602   1 EEKRIQQELARILNSFRDDPR-KKKNAVKKLLYLIMLGEDISFLFFEVVKLVASKDFTLKRLGYLYLMLLAEESPDLAIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  106 VTNSLKQDLNHTNQYIVGLALCALGNICSAEMARDLAPEVERLLQFRDPNIRKKAALCAIRIIRKVPDLSENFINPGAAL 185
Cdd:pfam01602  80 VTNSIQKDLQSPNQLIRGLALRTLSCIRVPELARDLAPDIKKLLVDRSPYVRKKAALAILKLYRKSPDLVRDFVPELKEL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  186 LKEKHHGVLITGVHLCTEICKVSSEALeyfrkKCTEGLVKTLRDIANspyspeydvagITDPFLHIRLLKLLRVLGQGD- 264
Cdd:pfam01602 160 LSDKDPGVQSAAVALLYEICKNDRLYL-----KLLPLLFRRLCNLLG-----------VLNPWLQVKILRLLTRLAPLDp 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  265 ADASDCMNDILAQVAsktesnkNAGNAILYECVQTIMSIEENGGLRVLAINILGKFLSNRDNNIRYVALNMLMRSLTVDS 344
Cdd:pfam01602 224 LLPKELLEDLLNLLQ-------NSNNAVLYETANTIVHLAPAPELIVLAVNALGRLLSSPDENLRYVALRNLNKIVMKEP 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  345 QAVQrHRATILECVK-DSDASIQKRALELIYLLVNENNVKPLAKELIEYL-EVSEQDFKGDLTAKICSIVEKFAPEKIWY 422
Cdd:pfam01602 297 KAVQ-HLDLIIFCLKtDDDISIRLRALDLLYALVNESNVKEIVKELLKYVhEIADPDFKIELVRAIGRLAEKFPTDAEWY 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  423 IDQMLKVLSEAGTYVKEDVWHALIVVITNAPDLHGYTVRALYRALHTSfEQETLVRVAIWCIGEYADLLVNNagmldled 502
Cdd:pfam01602 376 LDVLLDLLSLAGSYVVDEIVEVIRDIIQNVPELREYILEHLCELLEDI-ESPEALAAALWILGEYGELIPNG-------- 446
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  503 pitvteSDAVDVVENAI-KHHLSDVTTKAMALIALLKISSRFPSCS--ERVKSIIGQ--NKGSFVLELQQRSLEFSSVIQ 577
Cdd:pfam01602 447 ------SSPPDLLRSILeVFVLESAKVRAAALTALAKLGLTSPEETtqNLIIQLLLTlaTQDSLDLEVRDRAVEYLRLLS 520

                  ...
gi 145336886  578 KHQ 580
Cdd:pfam01602 521 LAD 523
Alpha_adaptinC2 smart00809
Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link ...
751-859 5.32e-33

Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Gamma-adaptin is a subunit of the golgi adaptor. Alpha adaptin is a heterotetramer that regulates clathrin-bud formation. The carboxyl-terminal appendage of the alpha subunit regulates translocation of endocytic accessory proteins to the bud site. This Ig-fold domain is found in alpha, beta and gamma adaptins and consists of a beta-sandwich containing 7 strands in 2 beta-sheets in a greek-key topology.. The adaptor appendage contains an additional N-terminal strand.


Pssm-ID: 197886 [Multi-domain]  Cd Length: 104  Bit Score: 122.74  E-value: 5.32e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886   751 AFESSSLKIEFNFTKQSENpqtTDIVANFINLTPNVYTEFLFQAAVPKFLQLHLDPASSNSLPANGNIKQTMRVTNsqKG 830
Cdd:smart00809   1 AYEKNGLQIGFKFERRPGL---IRITLTFTNKSPSPITNFSFQAAVPKSLKLQLQPPSSPTLPPGGQITQVLKVEN--PG 75
                           90       100
                   ....*....|....*....|....*....
gi 145336886   831 KKPIVMRMRVGYKINGKDVLEEGQINNFP 859
Cdd:smart00809  76 KFPLRLRLRLSYLLGGSAVTEQGDVLKFP 104
Alpha_adaptinC2 pfam02883
Adaptin C-terminal domain; Alpha adaptin is a heterotetramer which regulates clathrin-bud ...
747-859 1.28e-28

Adaptin C-terminal domain; Alpha adaptin is a heterotetramer which regulates clathrin-bud formation. The carboxyl-terminal appendage of the alpha subunit regulates translocation of endocytic accessory proteins to the bud site. This ig-fold domain is found in alpha, beta and gamma adaptins.


Pssm-ID: 460735  Cd Length: 111  Bit Score: 110.49  E-value: 1.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  747 PSIVAFESSSLKIEFNFTKqSENPQTTDIVANFINLTPNVYTEFLFQAAVPKFLQLHLDPASSNSLPANGN--IKQTMRV 824
Cdd:pfam02883   1 PPVVLYESDGLQIGFSFER-SRRPGQIRITLTFTNKSSSPISNFSFQAAVPKSLKLQLQPPSSNVLPPNPGgqITQVLLI 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 145336886  825 TNsqKGKKPIVMRMRVGYKiNGKDVLEEGQINNFP 859
Cdd:pfam02883  80 EN--PGKKPLRMRLKISYL-NGGAVQEQGDVLKFP 111
COG5096 COG5096
Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular ...
32-490 2.52e-09

Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 227427 [Multi-domain]  Cd Length: 757  Bit Score: 60.90  E-value: 2.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  32 KECAAIRASINENDQDYRHRDLAKLMFIHM-LGYPTHFGQMECLKLIASPGFPEKRIGYLGLMLLLDERQEVLMLVTNSL 110
Cdd:COG5096   18 DSVAALSSGRLESSNDYKKIDAMKKIIAQMsLGEDMSSLFPDVIKNVATRDVELKRLLYLYLERYAKLKPELALLAVNTI 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886 111 KQDLNHTNQYIVGLALCALGNICSAEMARDLAPEVERLLQFRDPNIRKKAALCAIRIIRKVPDL--SENFINPGAALLKE 188
Cdd:COG5096   98 QKDLQDPNEEIRGFALRTLSLLRVKELLGNIIDPIKKLLTDPHAYVRKTAALAVAKLYRLDKDLyhELGLIDILKELVAD 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886 189 KHHGVLITGVHLCTEICKvsSEALEYFRK--------------KCTEGLVKT-----LRDIANSPYSPEYDVAGITDPFL 249
Cdd:COG5096  178 SDPIVIANALASLAEIDP--ELAHGYSLEvilripqldllslsVSTEWLLLIilevlTERVPTTPDSAEDFEERLSPPLQ 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886 250 HirllkllrvlgqgdADASDCMN--DILAQVASKTESNKNAgnAILYECVQTIMSIEENGGLRVLAINILgKFLSNRDNn 327
Cdd:COG5096  256 H--------------NNAEVLLIavKVILRLLVFLPSNNLF--LISSPPLVTLLAKPESLIQYVLRRNIQ-IDLEVCSK- 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886 328 iryvALNMLMRsltvdsqavqrhratILECVKDSDASIQKRALELIYLLVNENNVKPLAKELIEY-------LEVSEQDF 400
Cdd:COG5096  318 ----LLDKVKK---------------LFLIEYNDDIYIKLEKLDQLTRLADDQNLSQILLELIYYiaenhidAEMVSEAI 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886 401 K--GDLTAKICSIVEKF----------APEKIWYIDQMlkvlSEAGTYVKEDVWHALIVVI--TNAPDLHGYTVRALYRA 466
Cdd:COG5096  379 KalGDLASKAESSVNDCisellellegVWIRGSYIVQE----VRIVDCISVIRISVLVLRIlpNEYPKILLRGLYALEET 454
                        490       500
                 ....*....|....*....|....*....
gi 145336886 467 L-HTSFEQE----TLVRVAIWCIGEYADL 490
Cdd:COG5096  455 LeLQSREPRaksvTDKYLGAWLLGEFSDI 483
KAR9 pfam08580
Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal ...
596-756 8.68e-03

Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal protein required for karyogamy, correct positioning of the mitotic spindle and for orientation of cytoplasmic microtubules. KAR9 localizes at the shmoo tip in mating cells and at the tip of the growing bud in anaphase.


Pssm-ID: 430088 [Multi-domain]  Cd Length: 684  Bit Score: 39.81  E-value: 8.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  596 ATFSGRRAGS--LPASVSTSGKSPLGIPNGVAKAAAPLvdllDLGSDDTPAPTSSSNnflqdlLGVDLSQPSAQPGAMQP 673
Cdd:pfam08580 448 KTPSSRRGSSfdFGSSSERVINSKLRRESKLPQIASTL----KQTKRPSKIPRASPN------HSGFLSTPSNTATSETP 517
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  674 SQAGADILMDLLSIGTPAPVQNGSANGDLLSIQDNNAPIAPSLTSPTaPSSMMDLLDGFGPTPPKSEDKSAAYPSIVAFE 753
Cdd:pfam08580 518 TPALRPPSRPQPPPPGNRPRWNASTNTNDLDVGHNFKPLTLTTPSPT-PSRSSRSSSTLPPVSPLSRDKSRSPAPTCRSV 596

                  ...
gi 145336886  754 SSS 756
Cdd:pfam08580 597 SRA 599
 
Name Accession Description Interval E-value
Adaptin_N pfam01602
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
26-580 3.42e-164

Adaptin N terminal region; This family consists of the N terminal region of various alpha, beta and gamma subunits of the AP-1, AP-2 and AP-3 adaptor protein complexes. The adaptor protein (AP) complexes are involved in the formation of clathrin-coated pits and vesicles. The N-terminal region of the various adaptor proteins (APs) is constant by comparison to the C-terminal which is variable within members of the AP-2 family; and it has been proposed that this constant region interacts with another uniform component of the coated vesicles.


Pssm-ID: 396262 [Multi-domain]  Cd Length: 523  Bit Score: 487.90  E-value: 3.42e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886   26 ERAVVRKECAAIRASINENDQdYRHRDLAKLMFIHMLGYPTHFGQMECLKLIASPGFPEKRIGYLGLMLLLDERQEVLML 105
Cdd:pfam01602   1 EEKRIQQELARILNSFRDDPR-KKKNAVKKLLYLIMLGEDISFLFFEVVKLVASKDFTLKRLGYLYLMLLAEESPDLAIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  106 VTNSLKQDLNHTNQYIVGLALCALGNICSAEMARDLAPEVERLLQFRDPNIRKKAALCAIRIIRKVPDLSENFINPGAAL 185
Cdd:pfam01602  80 VTNSIQKDLQSPNQLIRGLALRTLSCIRVPELARDLAPDIKKLLVDRSPYVRKKAALAILKLYRKSPDLVRDFVPELKEL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  186 LKEKHHGVLITGVHLCTEICKVSSEALeyfrkKCTEGLVKTLRDIANspyspeydvagITDPFLHIRLLKLLRVLGQGD- 264
Cdd:pfam01602 160 LSDKDPGVQSAAVALLYEICKNDRLYL-----KLLPLLFRRLCNLLG-----------VLNPWLQVKILRLLTRLAPLDp 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  265 ADASDCMNDILAQVAsktesnkNAGNAILYECVQTIMSIEENGGLRVLAINILGKFLSNRDNNIRYVALNMLMRSLTVDS 344
Cdd:pfam01602 224 LLPKELLEDLLNLLQ-------NSNNAVLYETANTIVHLAPAPELIVLAVNALGRLLSSPDENLRYVALRNLNKIVMKEP 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  345 QAVQrHRATILECVK-DSDASIQKRALELIYLLVNENNVKPLAKELIEYL-EVSEQDFKGDLTAKICSIVEKFAPEKIWY 422
Cdd:pfam01602 297 KAVQ-HLDLIIFCLKtDDDISIRLRALDLLYALVNESNVKEIVKELLKYVhEIADPDFKIELVRAIGRLAEKFPTDAEWY 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  423 IDQMLKVLSEAGTYVKEDVWHALIVVITNAPDLHGYTVRALYRALHTSfEQETLVRVAIWCIGEYADLLVNNagmldled 502
Cdd:pfam01602 376 LDVLLDLLSLAGSYVVDEIVEVIRDIIQNVPELREYILEHLCELLEDI-ESPEALAAALWILGEYGELIPNG-------- 446
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  503 pitvteSDAVDVVENAI-KHHLSDVTTKAMALIALLKISSRFPSCS--ERVKSIIGQ--NKGSFVLELQQRSLEFSSVIQ 577
Cdd:pfam01602 447 ------SSPPDLLRSILeVFVLESAKVRAAALTALAKLGLTSPEETtqNLIIQLLLTlaTQDSLDLEVRDRAVEYLRLLS 520

                  ...
gi 145336886  578 KHQ 580
Cdd:pfam01602 521 LAD 523
Alpha_adaptinC2 smart00809
Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link ...
751-859 5.32e-33

Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Gamma-adaptin is a subunit of the golgi adaptor. Alpha adaptin is a heterotetramer that regulates clathrin-bud formation. The carboxyl-terminal appendage of the alpha subunit regulates translocation of endocytic accessory proteins to the bud site. This Ig-fold domain is found in alpha, beta and gamma adaptins and consists of a beta-sandwich containing 7 strands in 2 beta-sheets in a greek-key topology.. The adaptor appendage contains an additional N-terminal strand.


Pssm-ID: 197886 [Multi-domain]  Cd Length: 104  Bit Score: 122.74  E-value: 5.32e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886   751 AFESSSLKIEFNFTKQSENpqtTDIVANFINLTPNVYTEFLFQAAVPKFLQLHLDPASSNSLPANGNIKQTMRVTNsqKG 830
Cdd:smart00809   1 AYEKNGLQIGFKFERRPGL---IRITLTFTNKSPSPITNFSFQAAVPKSLKLQLQPPSSPTLPPGGQITQVLKVEN--PG 75
                           90       100
                   ....*....|....*....|....*....
gi 145336886   831 KKPIVMRMRVGYKINGKDVLEEGQINNFP 859
Cdd:smart00809  76 KFPLRLRLRLSYLLGGSAVTEQGDVLKFP 104
Alpha_adaptinC2 pfam02883
Adaptin C-terminal domain; Alpha adaptin is a heterotetramer which regulates clathrin-bud ...
747-859 1.28e-28

Adaptin C-terminal domain; Alpha adaptin is a heterotetramer which regulates clathrin-bud formation. The carboxyl-terminal appendage of the alpha subunit regulates translocation of endocytic accessory proteins to the bud site. This ig-fold domain is found in alpha, beta and gamma adaptins.


Pssm-ID: 460735  Cd Length: 111  Bit Score: 110.49  E-value: 1.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  747 PSIVAFESSSLKIEFNFTKqSENPQTTDIVANFINLTPNVYTEFLFQAAVPKFLQLHLDPASSNSLPANGN--IKQTMRV 824
Cdd:pfam02883   1 PPVVLYESDGLQIGFSFER-SRRPGQIRITLTFTNKSSSPISNFSFQAAVPKSLKLQLQPPSSNVLPPNPGgqITQVLLI 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 145336886  825 TNsqKGKKPIVMRMRVGYKiNGKDVLEEGQINNFP 859
Cdd:pfam02883  80 EN--PGKKPLRMRLKISYL-NGGAVQEQGDVLKFP 111
COG5096 COG5096
Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular ...
32-490 2.52e-09

Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 227427 [Multi-domain]  Cd Length: 757  Bit Score: 60.90  E-value: 2.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  32 KECAAIRASINENDQDYRHRDLAKLMFIHM-LGYPTHFGQMECLKLIASPGFPEKRIGYLGLMLLLDERQEVLMLVTNSL 110
Cdd:COG5096   18 DSVAALSSGRLESSNDYKKIDAMKKIIAQMsLGEDMSSLFPDVIKNVATRDVELKRLLYLYLERYAKLKPELALLAVNTI 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886 111 KQDLNHTNQYIVGLALCALGNICSAEMARDLAPEVERLLQFRDPNIRKKAALCAIRIIRKVPDL--SENFINPGAALLKE 188
Cdd:COG5096   98 QKDLQDPNEEIRGFALRTLSLLRVKELLGNIIDPIKKLLTDPHAYVRKTAALAVAKLYRLDKDLyhELGLIDILKELVAD 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886 189 KHHGVLITGVHLCTEICKvsSEALEYFRK--------------KCTEGLVKT-----LRDIANSPYSPEYDVAGITDPFL 249
Cdd:COG5096  178 SDPIVIANALASLAEIDP--ELAHGYSLEvilripqldllslsVSTEWLLLIilevlTERVPTTPDSAEDFEERLSPPLQ 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886 250 HirllkllrvlgqgdADASDCMN--DILAQVASKTESNKNAgnAILYECVQTIMSIEENGGLRVLAINILgKFLSNRDNn 327
Cdd:COG5096  256 H--------------NNAEVLLIavKVILRLLVFLPSNNLF--LISSPPLVTLLAKPESLIQYVLRRNIQ-IDLEVCSK- 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886 328 iryvALNMLMRsltvdsqavqrhratILECVKDSDASIQKRALELIYLLVNENNVKPLAKELIEY-------LEVSEQDF 400
Cdd:COG5096  318 ----LLDKVKK---------------LFLIEYNDDIYIKLEKLDQLTRLADDQNLSQILLELIYYiaenhidAEMVSEAI 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886 401 K--GDLTAKICSIVEKF----------APEKIWYIDQMlkvlSEAGTYVKEDVWHALIVVI--TNAPDLHGYTVRALYRA 466
Cdd:COG5096  379 KalGDLASKAESSVNDCisellellegVWIRGSYIVQE----VRIVDCISVIRISVLVLRIlpNEYPKILLRGLYALEET 454
                        490       500
                 ....*....|....*....|....*....
gi 145336886 467 L-HTSFEQE----TLVRVAIWCIGEYADL 490
Cdd:COG5096  455 LeLQSREPRaksvTDKYLGAWLLGEFSDI 483
SEC21 COG5240
Vesicle coat complex COPI, gamma subunit [Intracellular trafficking and secretion];
38-667 4.60e-04

Vesicle coat complex COPI, gamma subunit [Intracellular trafficking and secretion];


Pssm-ID: 227565 [Multi-domain]  Cd Length: 898  Bit Score: 43.83  E-value: 4.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  38 RASINENDQDYRHRDLAKLMFIHMLGYPTHFGQMEC-------LKLIASPGFPEKRIGYLGLMLLLDERQEVLMlVTNSL 110
Cdd:COG5240   28 NESFNKSPVSTRSARKLLSNLFYLLSTGELFPEATAtnlffaiLKLFQHKDLYLRQCVYSAIKELSKLTEDVLM-GTSSI 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886 111 KQDLNHTNQYIV-GLALCALGNICSAEMArdlaPEVERLLQ--FRDPNI-RKKAALC--------AIRIIRK-VPDLSEN 177
Cdd:COG5240  107 MKDLNGGVPDDVkPMAIRSLFSVIDGETV----YDFERYLNqaFVSTSMaRRSAALVvayhllpnNFNQTKRwLNETQEA 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886 178 FINPGAALLKEKHHGVLITGvhlcTEICKVSSEALEYFRKKCTEGLVKTLRDIANSPYSPEYDVAGITdpflhirLLKLL 257
Cdd:COG5240  183 VLDLKQFPNQHGNEGYEPNG----NPISQYHALGLLYQSKRTDKMAQLKLVEHFRGNASMKNQLAGVL-------LVRAT 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886 258 RVLGQGDADASDCMNDILAQVASktesnkNAGNAILYECVQTIMSI-EENGGLRVL--AINILGKFLSNRDNNIRYVALN 334
Cdd:COG5240  252 VELLKENSQALLQLRPFLNSWLS------DKFEMVFLEAARAVCALsEENVGSQFVdqTVSSLRTFLKSTRVVLRFSAMR 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886 335 MLMRSLTVDSQAVQRHRATILECVKDSDASIQKRALELIYLLVNENNVKPLAKELIEYLEVSEQDFKGDLTAKICSIVEK 414
Cdd:COG5240  326 ILNQLAMKYPQKVSVCNKEVESLISDENRTISTYAITTLLKTGTEETIDRLVNLIPSFVHDMSDGFKIIAIDALRSLSLL 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886 415 FAPEKIWYIDQMLKVLSEAGTY-VKEDVWHALIVVITNAPDLHgytvralYRALhtsfeqETLVRVAIWCigEYADLLVN 493
Cdd:COG5240  406 FPSKKLSYLDFLGSSLLQEGGLeFKKYMVDAISDAMENDPDSK-------ERAL------EVLCTFIEDC--EYHQITVR 470
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886 494 NAGMLDLEDPITVTESDAVDVVENAIKhhLSDVTTKAMALIALLK--ISSRFPSCSERVKSIIG----------QNKGSF 561
Cdd:COG5240  471 ILGILGREGPRAKTPGKYVRHIYNRLI--LENNIVRSAAVQALSKfaLNISDVVSPQSVENALKrclndqddevRDRASF 548
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886 562 VLELQQRSLEFSSVIQ--KHQNIRSSLVERMPVLDEATFSgrrAGSLPASVSTSGKSPLGIPNGVAKAAAPLVDLLDLGS 639
Cdd:COG5240  549 LLRNMRLSDACEPLFSsdELGDIPSLELELIGYISEDSFA---TAFDVNQVRKFTEDEMKAINLKRKKSETTLDTTESVP 625
                        650       660       670
                 ....*....|....*....|....*....|.
gi 145336886 640 DDTPAPTSSSN---NFLQDLLGVDLSQPSAQ 667
Cdd:COG5240  626 KEDANSKADPNiktKYADELLSIEQIKPFGQ 656
KAR9 pfam08580
Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal ...
596-756 8.68e-03

Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal protein required for karyogamy, correct positioning of the mitotic spindle and for orientation of cytoplasmic microtubules. KAR9 localizes at the shmoo tip in mating cells and at the tip of the growing bud in anaphase.


Pssm-ID: 430088 [Multi-domain]  Cd Length: 684  Bit Score: 39.81  E-value: 8.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  596 ATFSGRRAGS--LPASVSTSGKSPLGIPNGVAKAAAPLvdllDLGSDDTPAPTSSSNnflqdlLGVDLSQPSAQPGAMQP 673
Cdd:pfam08580 448 KTPSSRRGSSfdFGSSSERVINSKLRRESKLPQIASTL----KQTKRPSKIPRASPN------HSGFLSTPSNTATSETP 517
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145336886  674 SQAGADILMDLLSIGTPAPVQNGSANGDLLSIQDNNAPIAPSLTSPTaPSSMMDLLDGFGPTPPKSEDKSAAYPSIVAFE 753
Cdd:pfam08580 518 TPALRPPSRPQPPPPGNRPRWNASTNTNDLDVGHNFKPLTLTTPSPT-PSRSSRSSSTLPPVSPLSRDKSRSPAPTCRSV 596

                  ...
gi 145336886  754 SSS 756
Cdd:pfam08580 597 SRA 599
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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